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Journal of the Japanese Society of Starch Science最新文献

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Synthesis of Fructan and Oligosaccharides by Microbial and Plant Fructosyltransf erasest 利用微生物和植物果糖转移酶合成果聚糖和低聚糖
Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.217
M. Iizuka, Toshio Tanaka, Satoru Yamamoto, Y. Yoneda, S. Itokawa, M. Hiyama, K. Furuichi, N. Minamiura, Takehiko Yamamoto
{"title":"Synthesis of Fructan and Oligosaccharides by Microbial and Plant Fructosyltransf erasest","authors":"M. Iizuka, Toshio Tanaka, Satoru Yamamoto, Y. Yoneda, S. Itokawa, M. Hiyama, K. Furuichi, N. Minamiura, Takehiko Yamamoto","doi":"10.5458/JAG1972.38.217","DOIUrl":"https://doi.org/10.5458/JAG1972.38.217","url":null,"abstract":"It was observed that a considerable amount of fructosyltransferase, levansucrase, was produced when microorganisms (Bacillus subtilis, Bacillus natto, Zymomonas mobilis, etc.) were grown on a medium containing sucrose and the activity was found in culture filtrate and cells. But most of the activity was retained by the cells together with viscous levan in the case of Bacillus natto. The cells harvested and washed with buffer after cultivation were able to be used as reactors repeatedly for the production of levan by soaking in sucrose solution. A complete liberation of the enzyme from the cells was achieved by treating with 2 M sodium chloride solution. Oligosaccharides synthesized from sucrose in the presence of some acceptor sugars were useful for screening of microorganisms which produce exo-type carbohydrases such as a-glucosidase. Low molecular weight levan synthesized under the condition of high concentration of sodium chloride (2 M) was also useful for screening the microorganisms which produced levanbiose-producing enzyme because of its few branchings. The low molecular levan may be useful as a carbon source for finding enzyme having special specificity such as producing cyclic f ructan. Sucrase (β-fructofuranosidase) obtained from microorganisms produced mainly 1-kestose except yeast invertase, which produced mainly 6-kestose; levansucrase produced three types of kestose (1-kestose, neokestose and 6-kestose) and levan, regardless of enzyme source.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"7 1","pages":"217-222"},"PeriodicalIF":0.0,"publicationDate":"1991-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79013208","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 9
Differentiation of Novel Human α-Amylase from Salivary and Pancreatic α-Amylases 新型人α-淀粉酶与唾液和胰腺α-淀粉酶的分化
Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.193
K. Omichi, K. Shiosaki, K. Matsubara, T. Ikenaka
{"title":"Differentiation of Novel Human α-Amylase from Salivary and Pancreatic α-Amylases","authors":"K. Omichi, K. Shiosaki, K. Matsubara, T. Ikenaka","doi":"10.5458/JAG1972.38.193","DOIUrl":"https://doi.org/10.5458/JAG1972.38.193","url":null,"abstract":"yHXA is the gene product of a newly found human a-amylase gene (AMY2B) expressed in yeast. Its mode of action on a derivative of p-nitrophenyl ƒ¿-maltopentaoside, FG5P (FG-G-G-GG-P), was compared with those of the ƒ¿-amylases (yHSA, yHPA), which were produced by expression of human salivary and pancreatic ƒ¿-amylase genes (AMY1 , AMY2A) in yeast. The product analysis of the digests by HPLC showed that the enzymes hydrolyzed FG5P to FG3 (FG-G-G) and p-nitrophenyl a-maltoside (G-G-P) and to FG4 (FG-G-G-G) and p-nitrophenyl ƒ¿-glucoside (G-P) , and the ratio of the two reactions changed with pH. The three enzymes differed from each other in the mode of action at pH 5.5. The molar ratio of FG4 to FG3 in the digest with yHXA was the largest and that with yHSA was the least.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"36 1","pages":"193-196"},"PeriodicalIF":0.0,"publicationDate":"1991-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81970489","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Structure and Catalytic Implications of Taka-Amylase A 塔卡淀粉酶A的结构及其催化意义
Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.137
Y. Matsuura, M. Kusunoki, M. Kakudo
{"title":"Structure and Catalytic Implications of Taka-Amylase A","authors":"Y. Matsuura, M. Kusunoki, M. Kakudo","doi":"10.5458/JAG1972.38.137","DOIUrl":"https://doi.org/10.5458/JAG1972.38.137","url":null,"abstract":"Taka-amylase has a (αβ)8 barrel structure and the active site is located at the C-terminal end of a β-strand as reported earlier. In this paper, we describe about the direction of substrate amylose binding with respect to the barrel structure. A possible mechanism of hydrolysis is also proposed, in which Glu 230, Asp 297 and Asp 206 located near the active site are essentially involved.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"33 1","pages":"137-139"},"PeriodicalIF":0.0,"publicationDate":"1991-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72546254","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 13
Specific 3A, 3C, 3E-0-Trisulfonylation of β-cyclodextrin 特异性3A, 3C, 3e -0-三磺化β-环糊精
Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.205
K. Fujita, T. Tahara, H. Yamamura, T. Koga
{"title":"Specific 3A, 3C, 3E-0-Trisulfonylation of β-cyclodextrin","authors":"K. Fujita, T. Tahara, H. Yamamura, T. Koga","doi":"10.5458/JAG1972.38.205","DOIUrl":"https://doi.org/10.5458/JAG1972.38.205","url":null,"abstract":"3A, 3C, 3E-O-tris(β-naphthylsulfonyl)-β-cyclodextrin was selectively prepared by the reaction of β-cyclodextrin with β-naphthylsulfonyl chloride in an alkaline solution. The structure determination was carried out by use of a regiochemical relationship between a 3-O-sulfonylcyclodextrin with a 6-O-sulfonylcyclodextrin through a 3, 6-anhydrocyclodextrin.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"136 1","pages":"205-209"},"PeriodicalIF":0.0,"publicationDate":"1991-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89245349","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Production and Some Properties of Branched Cyclodextrins 支化环糊精的制备及其性质
Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.197
S. Kobayashi, K. Nakashima, M. Arahira
{"title":"Production and Some Properties of Branched Cyclodextrins","authors":"S. Kobayashi, K. Nakashima, M. Arahira","doi":"10.5458/JAG1972.38.197","DOIUrl":"https://doi.org/10.5458/JAG1972.38.197","url":null,"abstract":"Cyclodextrins (CDs, tt cyclomaltooligosaccharides) with maltosyl and panosyl branches were produced from maltose or panose and CDs by the reverse action of pullulanase. Purification on columns of octadesylated silica gave G2-α-CD, G2-β-CD, Pan-α-CD, and Pan-β-CD. The solubility of G2-β-CD in aqueous 80% ethanol was higher than that of β-CD in water. The relative rates of degradation of maltose, G2-α-CD, and G2-β-CD with glucoamylase were 1 : 3.6 : 5.0 and those of panose, Pan-α-CD, and Pan-β-CD were 1 : 3.0 : 2.2. The rates of degradation of branched and unbranched maltooligosaccharides were markedly different from those of G2-CDs and Pan-CDs.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"28 1","pages":"197-200"},"PeriodicalIF":0.0,"publicationDate":"1991-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87000686","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 2
Chemically Modified Starches 化学改性淀粉
Journal of the Japanese Society of Starch Science Pub Date : 1991-03-31 DOI: 10.5458/JAG1972.38.55
Masao Shimashita
{"title":"Chemically Modified Starches","authors":"Masao Shimashita","doi":"10.5458/JAG1972.38.55","DOIUrl":"https://doi.org/10.5458/JAG1972.38.55","url":null,"abstract":"Chemically modified starches are widely used for Paper, Textile and Food Industries, etc. This paper explains the basic properties and uses of chemically modified starches .","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"38 1","pages":"55-63"},"PeriodicalIF":0.0,"publicationDate":"1991-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81215195","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 3
Characterization of food melanoidin. 食品类黑素的表征。
Journal of the Japanese Society of Starch Science Pub Date : 1991-03-31 DOI: 10.5458/JAG1972.38.73
S. Homma
{"title":"Characterization of food melanoidin.","authors":"S. Homma","doi":"10.5458/JAG1972.38.73","DOIUrl":"https://doi.org/10.5458/JAG1972.38.73","url":null,"abstract":"Melanoidin is a colored substance which is generally found in food system. Its formation mechanism has been mostly studied by model systems which consist of reducing sugar and amino acid. The author proposes a few methods to characterize melanoidin in food system. Electrofocusing profile of soy sauce melanoidin was found to be similar to that of the model melanoidin. Fe(‡U) chelating Sepharose 6B column chromatography of soy gave a proof of the presence of polyphenolic-type melanoidin which was adsorbed to the Fe (II) -column with strong affinity. Coffee melanoidin was adsorbed to the Cu (II) -column with stronger affinity than soy sauce melanoidin. Food melanoidins were categorized into 3 groups by microbial degradation using Coriolus versicolor. Model melanoidin, soy sauce and cane, molasses were characterized by reduction of color intensity by more than 50%; cocoa was characterized by adsorption of the melanoidin to the cell surface; coffee was almost stable against the microbial degradation.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"77 1","pages":"73-79"},"PeriodicalIF":0.0,"publicationDate":"1991-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74448330","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 1
Browning in Processed Foods 加工食品中的褐变
Journal of the Japanese Society of Starch Science Pub Date : 1991-03-31 DOI: 10.5458/JAG1972.38.93
K. Ishiguro, M. Yonemitsu
{"title":"Browning in Processed Foods","authors":"K. Ishiguro, M. Yonemitsu","doi":"10.5458/JAG1972.38.93","DOIUrl":"https://doi.org/10.5458/JAG1972.38.93","url":null,"abstract":"Browning reaction causes a qualitative change of processed foods not only in color but also in taste, flavor, nutritive value etc. Therefore it is important to control the browning reaction in food processing. Control of browning reaction in several processed foods during processing and storage is discussed. They are as follows. (1) Repression of browning by decreasing of participating substances in amino carbonyl reactions. (2) Calculation of integrated browning degree by use of Arrhenius' equation and control of browning at the thermal process by the calculated browning degree. (3) Effect of temperature, oxygen and moisture on browning during storage.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"13 1","pages":"93-98"},"PeriodicalIF":0.0,"publicationDate":"1991-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84294431","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Substrate Binding Site of Streptomyces Xylose Isomerase, Studied by the Fluorescence Spectrophotometry Using Xylose and Xylitol 用木糖和木糖醇荧光分光光度法研究链霉菌木糖异构酶的底物结合位点
Journal of the Japanese Society of Starch Science Pub Date : 1991-03-31 DOI: 10.5458/JAG1972.38.41
M. Ohnishi, Y. Fujioka, Shigeo Takewuti, T. Yoshida, C. Hashizume, K. Hiromi, B. Tonomura
{"title":"Substrate Binding Site of Streptomyces Xylose Isomerase, Studied by the Fluorescence Spectrophotometry Using Xylose and Xylitol","authors":"M. Ohnishi, Y. Fujioka, Shigeo Takewuti, T. Yoshida, C. Hashizume, K. Hiromi, B. Tonomura","doi":"10.5458/JAG1972.38.41","DOIUrl":"https://doi.org/10.5458/JAG1972.38.41","url":null,"abstract":"Binding of a substrate xylose to Streptomyces xylose isomerase (XIase) was observed by using a change (decrease) in fluorescence intensity (based on tryptophan residue) as a probe, and the binding parameters Kb and ΔFmax were evaluated for the xylose-XIase complex formation. An analogue xylitol was found not to produce the change in fluorescence intensity ; never theless, it competitively inhibits the XIase-catalyzed reaction for a substrate xylose . These findings suggest that the tryptophan residue (s) is located at the binding site of xylose to interact with some group of the xylose molecule, of which group is missing in xylitol . eq-Glucose, α-glucose and fructose were confirmed to be bound into XIase as a substrate, whereas IS-glucose was certified not to be a substrate of the enzyme.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"2015 1","pages":"41-44"},"PeriodicalIF":0.0,"publicationDate":"1991-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87249492","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Relative Length of Exterior and Interior Chain of the Phytoglycogen from Italian Millet 意大利谷子植物糖原外链和内链的相对长度
Journal of the Japanese Society of Starch Science Pub Date : 1991-03-31 DOI: 10.5458/JAG1972.38.23
Koji Kato, S. Makino, R. Yamauchi, Y. Ueno
{"title":"Relative Length of Exterior and Interior Chain of the Phytoglycogen from Italian Millet","authors":"Koji Kato, S. Makino, R. Yamauchi, Y. Ueno","doi":"10.5458/JAG1972.38.23","DOIUrl":"https://doi.org/10.5458/JAG1972.38.23","url":null,"abstract":"アワ種子胚乳部のフィトグリコーゲンおよびそのβ-リミットデキストリン(β-LD)をα-アミラーゼで分解した.各分解液中の分岐オリゴ糖に対するグルコース,マルトースおよびマルトトリオースの合計量を求めたところ,フィトグリコーゲンでは0.68,β-LDでは0.12となった.これらの値から,このフィトグリコーゲンの外部鎖は内部鎖に比べ4～5倍長いということが推定された.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"30 1","pages":"23-26"},"PeriodicalIF":0.0,"publicationDate":"1991-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74793579","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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